Archana Prasad

TL;DR: The roles of TDP-43's mutations, its cytoplasmic mis-localization and aberrant post-translational modifications in ALS, its amyloid-like in vitro aggregation, its physiological vs. pathological oligomerization in vivo, liquid-liquid phase separation (LLPS), and potential prion-like propagation propensity of the TDP -43 inclusions are discussed.

TL;DR: Among several acridine derivatives examined, AIM4, which contains polar carboxyl groups in the side arms, significantly reduces TDP-43-YFP aggregation in the powerful yeast model cell and also abolishes in vitro amyloid-like aggregation of car boxyl terminal domain of TDP -43, as observed by AFM imaging.

TL;DR: It is hypothesize that amyloid‐induced oxidative stress would deplete reduced‐glutathione levels and thus thwart the development of red colour in ade1 or ade2 yeast.

TL;DR: It is found that kosmotropic anions greatly accelerate whereas chaotropic anions impede its aggregation, and acetylation of certain lysines in C-terminal fragments significantly reduces the TDP-432C's amyloid-like aggregation.

TL;DR: It is found that HEWL aggregates formed under quiescent versus agitated conditions, displayed different particle sizes, detergent stabilities & β-sheet content, and they only seeded monomeric H EWL under similar incubation conditions, thereby showing amyloid variant formation by HewL analogous to prion variants, which may have implications to the amyloids caused by different mutants of human lysozyme.